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Tailoring the pH dependence of enzyme catalysis using protein engineering

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Tailoring the pH dependence of enzyme catalysis using protein engineering (English)

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3

Alan R. Fersht

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Paul G. Thomas

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1

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Alan J. Russell

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2

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English

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publication date

November 1985

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Nature

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318

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6044

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page(s)

375-376

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cites work

Kinetic properties of succinylated and ethylenediamine-amidated δ-chymotrypsins

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Electrostatic effects in proteins

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Macroscopic models for studies of electrostatic interactions in proteins: limitations and applicability

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Electrostatic effects in hemoglobin: hydrogen ion equilibria in human deoxy- and oxyhemoglobin A

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[Primary structure of subtilisin DY]

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Restriction maps of plasmids pUB110 and pBD9

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DNA sequencing with chain-terminating inhibitors

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Cloning, sequencing, and secretion of Bacillusamyloliquefacienssubtillisin inBacillus subtilis

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Comparison of the kinetic specificity of subtilisin and thiolsubtilisin toward n-alkyl p-nitrophenyl esters

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32 Oligonucleotide-directed mutagenesis of DNA fragments cloned into M13 vectors

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Redesigning enzyme structure by site-directed mutagenesis: tyrosyl tRNA synthetase and ATP binding

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Different base/base mismatches are corrected with different efficiencies by the methyl-directed DNA mismatch-repair system of E. coli

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pH Dependence of chymotrypsin catalysis. Appendix. Substrate binding to dimeric α-chymotrypsin studied by x-ray diffraction and the equilibrium method

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The Determination of the Concentration of Hydrolytic Enzyme Solutions: α-Chymotrypsin, Trypsin, Papain, Elastase, Subtilisin, and Acetylcholinesterase1

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10.1038/318375A0

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1046764988

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(Q59066057)

Tailoring the pH dependence of enzyme catalysis using protein engineering

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